Abstract
Rat ventral prostate nucleoli contain protein phosphokinase(s) which have distinctly different characteristics from protein phosphokinase(s) localized in the extra-nucleolar regions of the nucleus. The differences pertain to pH vs activity profiles and activation by divalent cations, utilizing dephospho-phosvitin as substrate. Lysine-rich and arginine-rich F3 histones are also phosphorylated by nucleolar protein phosphokinase(s). Phosphorylation of histones by either nucleolar or extra-nucleolar fractions was not stimulated by cAMP, whereas that of phosvitin was slightly inhibited.
Original language | English (US) |
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Pages (from-to) | 261-266 |
Number of pages | 6 |
Journal | Experimental Cell Research |
Volume | 93 |
Issue number | 2 |
DOIs | |
State | Published - Jul 1975 |